Caseinolytic mitochondrial matrix peptidase proteolytic subunit (ClpP)

ClpP (Caseinolytic mitochondrial matrix peptidase proteolytic subunit) is a highly conserved serine protease found in bacteria, mitochondria of eukaryotes, and some chloroplasts. In humans, it is encoded by the *CLPP* gene and plays a critical role in protein quality control by degrading misfolded or damaged proteins within the mitochondrial matrix. It functions as part of larger ATP-dependent proteolytic complexes such as ClpXP or ClpAP. In bacteria, it's critical for stress response, virulence regulation, cell cycle progression, and adaptation to environmental changes. In humans, mutations in *CLPP* are associated with Perrault syndrome type 3 (PRLTS3). It has emerged as an anti-cancer target because its activation can induce selective cancer cell death via disruption of mitochondrial function and bacterial ClpPs are targets for novel antibiotics.

Other names

PRLTS3DFNB81

Activation of ClpP induces cancer cell death via disruption of mitochondrial function; inhibition of bacterial ClpP disrupts bacterial pathogenicity.